ID NCPR2_ARATH Reviewed; 711 AA. AC Q9SUM3; F4JPK2; Q39036; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 152. DE RecName: Full=NADPH--cytochrome P450 reductase 2 {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=CPR 2 {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=P450R 2 {ECO:0000255|HAMAP-Rule:MF_03212}; DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212}; GN Name=ATR2; Synonyms=AR2; OrderedLocusNames=At4g30210; GN ORFNames=F9N11.60; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RC STRAIN=cv. Landsberg erecta; RX PubMed=9235908; DOI=10.1074/jbc.272.31.19176; RA Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.; RT "Cloning, yeast expression, and characterization of the coupling of two RT distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases RT with P450 CYP73A5."; RL J. Biol. Chem. 272:19176-19186(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. RX PubMed=9990323; DOI=10.1046/j.1432-1327.1998.2581040.x; RA Louerat-Oriou B., Perret A., Pompon D.; RT "Differential redox and electron-transfer properties of purified yeast, RT plant and human NADPH-cytochrome P-450 reductases highly modulate RT cytochrome P-450 activities."; RL Eur. J. Biochem. 258:1040-1049(1998). RN [6] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=9449848; DOI=10.1104/pp.116.1.357; RA Mizutani M., Ohta D.; RT "Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. RT Gene structure, heterologous expression in insect cells, and differential RT regulation."; RL Plant Physiol. 116:357-367(1998). RN [7] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9880378; DOI=10.1104/pp.119.1.353; RA Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.; RT "Microsomal electron transfer in higher plants: cloning and heterologous RT expression of NADH-cytochrome b5 reductase from Arabidopsis."; RL Plant Physiol. 119:353-361(1999). RN [8] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10733884; DOI=10.1006/prep.1999.1195; RA Hull A.K., Celenza J.L.; RT "Bacterial expression and purification of the Arabidopsis NADPH-cytochrome RT P450 reductase ATR2."; RL Protein Expr. Purif. 18:310-315(2000). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Columbia; RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004; RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., RA Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis RT thaliana."; RL J. Proteomics 72:439-451(2009). CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to CC cytochrome P450 in microsomes. It can also provide electron transfer to CC heme oxygenase and cytochrome B5. Reduces a variety of substrates in CC vitro, such as cytochrome c, feericyanide and dichloroindophenol. CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:10733884, CC ECO:0000269|PubMed:9235908, ECO:0000269|PubMed:9449848, CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA- CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000269|PubMed:9990323}; CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212, ECO:0000269|PubMed:9990323}; CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23 uM for NADPH (at pH 7.7 and 28 degrees Celsius) CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848, CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}; CC KM=2 uM for NADPH (at pH 7.25 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848, CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}; CC KM=15 uM for cytochrome c (at pH 7.7 and 30 degrees Celsius) CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848, CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}; CC KM=16 uM for cytochrome c (at pH 7.0 and 25 degrees Celsius) CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848, CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}; CC KM=22.5 uM for cytochrome c (at pH 7.7 and 28 degrees Celsius) CC {ECO:0000269|PubMed:10733884, ECO:0000269|PubMed:9449848, CC ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_03212}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9SUM3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9SUM3-2; Sequence=VSP_042906; CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and CC siliques. {ECO:0000269|PubMed:9449848}. CC -!- INDUCTION: By wounding and transition from dark to light. CC {ECO:0000269|PubMed:9449848}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family. CC {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP- CC Rule:MF_03212}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X66017; CAA46815.1; -; mRNA. DR EMBL; AL109796; CAB52465.1; -; Genomic_DNA. DR EMBL; AL161576; CAB81014.1; -; Genomic_DNA. DR EMBL; CP002687; AEE85737.1; -; Genomic_DNA. DR EMBL; CP002687; AEE85738.1; -; Genomic_DNA. DR EMBL; AF325101; AAK17169.1; -; mRNA. DR PIR; S21531; S21531. DR PIR; T14081; T14081. DR RefSeq; NP_194750.1; NM_119167.4. [Q9SUM3-1] DR RefSeq; NP_849472.2; NM_179141.2. [Q9SUM3-2] DR PDB; 5GXU; X-ray; 2.30 A; A/B=73-711. DR PDBsum; 5GXU; -. DR AlphaFoldDB; Q9SUM3; -. DR SMR; Q9SUM3; -. DR STRING; 3702.Q9SUM3; -. DR iPTMnet; Q9SUM3; -. DR PaxDb; 3702-AT4G30210-1; -. DR ProteomicsDB; 251241; -. [Q9SUM3-1] DR EnsemblPlants; AT4G30210.1; AT4G30210.1; AT4G30210. [Q9SUM3-2] DR EnsemblPlants; AT4G30210.2; AT4G30210.2; AT4G30210. [Q9SUM3-1] DR GeneID; 829144; -. DR Gramene; AT4G30210.1; AT4G30210.1; AT4G30210. [Q9SUM3-2] DR Gramene; AT4G30210.2; AT4G30210.2; AT4G30210. [Q9SUM3-1] DR KEGG; ath:AT4G30210; -. DR Araport; AT4G30210; -. DR TAIR; AT4G30210; ATR2. DR eggNOG; KOG1158; Eukaryota. DR HOGENOM; CLU_001570_17_3_1; -. DR InParanoid; Q9SUM3; -. DR PhylomeDB; Q9SUM3; -. DR BioCyc; ARA:AT4G30210-MONOMER; -. DR BioCyc; MetaCyc:AT4G30210-MONOMER; -. DR SABIO-RK; Q9SUM3; -. DR PRO; PR:Q9SUM3; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9SUM3; baseline and differential. DR GO; GO:0009507; C:chloroplast; ISS:TAIR. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB. DR GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:UniProtKB. DR CDD; cd06204; CYPOR; 1. DR DisProt; DP02644; -. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_03212; NCPR; 1. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR023208; P450R. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000208; P450R; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR Genevisible; Q9SUM3; AT. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Endoplasmic reticulum; FAD; KW Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; KW Phenylpropanoid metabolism; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..711 FT /note="NADPH--cytochrome P450 reductase 2" FT /id="PRO_0000416840" FT TOPO_DOM 1..51 FT /note="Lumenal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT TRANSMEM 52..72 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT TOPO_DOM 73..711 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 105..255 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 310..556 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 111..116 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 166..169 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 204..213 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 239 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 330 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 489..492 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 507..509 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 523..526 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 570 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 631..632 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 637..641 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 673 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 711 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT VAR_SEQ 447 FT /note="K -> KV (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_042906" FT CONFLICT 297..298 FT /note="NM -> TL (in Ref. 1; CAA46815)" FT /evidence="ECO:0000305" FT CONFLICT 346..348 FT /note="YET -> MKL (in Ref. 1; CAA46815)" FT /evidence="ECO:0000305" FT CONFLICT 540..544 FT /note="NCSSA -> KLFLGR (in Ref. 1; CAA46815)" FT /evidence="ECO:0000305" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 115..130 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 141..144 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 148..155 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 159..168 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 178..185 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 198..205 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 214..225 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 243..259 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 313..322 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 332..338 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 360..370 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 403..409 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 419..426 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 432..442 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 447..453 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 454..458 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 461..467 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 475..478 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 479..482 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 489..492 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 497..499 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 501..509 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 524..531 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 563..566 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 569..572 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 573..586 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 587..589 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 595..602 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 604..606 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 611..619 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 624..635 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 640..646 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 648..656 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 660..665 FT /evidence="ECO:0007829|PDB:5GXU" FT TURN 667..669 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 670..686 FT /evidence="ECO:0007829|PDB:5GXU" FT HELIX 690..703 FT /evidence="ECO:0007829|PDB:5GXU" FT STRAND 705..710 FT /evidence="ECO:0007829|PDB:5GXU" SQ SEQUENCE 711 AA; 78927 MW; F0503108EB7F508F CRC64; MSSSSSSSTS MIDLMAAIIK GEPVIVSDPA NASAYESVAA ELSSMLIENR QFAMIVTTSI AVLIGCIVML VWRRSGSGNS KRVEPLKPLV IKPREEEIDD GRKKVTIFFG TQTGTAEGFA KALGEEAKAR YEKTRFKIVD LDDYAADDDE YEEKLKKEDV AFFFLATYGD GEPTDNAARF YKWFTEGNDR GEWLKNLKYG VFGLGNRQYE HFNKVAKVVD DILVEQGAQR LVQVGLGDDD QCIEDDFTAW REALWPELDT ILREEGDTAV ATPYTAAVLE YRVSIHDSED AKFNDINMAN GNGYTVFDAQ HPYKANVAVK RELHTPESDR SCIHLEFDIA GSGLTYETGD HVGVLCDNLS ETVDEALRLL DMSPDTYFSL HAEKEDGTPI SSSLPPPFPP CNLRTALTRY ACLLSSPKKS ALVALAAHAS DPTEAERLKH LASPAGKDEY SKWVVESQRS LLEVMAEFPS AKPPLGVFFA GVAPRLQPRF YSISSSPKIA ETRIHVTCAL VYEKMPTGRI HKGVCSTWMK NAVPYEKSEN CSSAPIFVRQ SNFKLPSDSK VPIIMIGPGT GLAPFRGFLQ ERLALVESGV ELGPSVLFFG CRNRRMDFIY EEELQRFVES GALAELSVAF SREGPTKEYV QHKMMDKASD IWNMISQGAY LYVCGDAKGM ARDVHRSLHT IAQEQGSMDS TKAEGFVKNL QTSGRYLRDV W //